Browsing by Author "201-0335298"
Now showing items 1-20 of 50
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(2007)FtsZ (Filamentous temperature sensitivity Z) cell division protein from Escherichia coli binds the fluorescence probe DAPI. Bundling of FtsZ was facilitated in the presence of DAPI, and the polymers in solution remained ...
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(BioMed Central Ltd., 2011)Background: Bacterial division is produced by the formation of a macromolecular complex in the middle of the cell, called the divisome, formed by more than 10 proteins. This process can be divided into two steps, in which ...
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(2009)The HCV internal ribosome entry site (IRES) spans a region of ∼340 nt that encompasses most of the 5′ untranslated region (5′UTR) of the viral mRNA and the first 24-40 nt of the core-coding region. To investigate the ...
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(1996)Nuclear magnetic resonance (NMR) spectroscopy is emerging as a powerful tool for the study of enzyme structure and function. This article discusses the general principles of NMR and the potential information this technique ...
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(Elsevier, 2014)Proteins involved in bacterial cell division often do not have a counterpart in eukaryotic cells and they are essential for the survival of the bacteria. The genetic accessibility of many bacterial species in combination with ...
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(American Society for Microbiology, 2017)Bacteria of the genus Prosthecobacter express homologs of eukaryotic alpha- and beta-tubulin, called BtubA and BtubB (BtubA/B), that have been observed to assemble into filaments in the presence of GTP. BtubA/B polymers ...
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(Universidad de Chile, 2011)Gran variedad de procesos industriales basados en reacciones catalizadas químicamente han sido reemplazados durante las últimas décadas por procesos biotecnológicos que involucran enzimas. En particular, el uso de enzimas ...
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Binding of dihydroxynaphthyl aryl ketones to tubulin colchicine site inhibits microtubule assembly (Elsevier, 2015)Dihydroxynaphthyl aryl ketones 1e5 have been evaluated for their abilities to inhibit microtubule assembly and the binding to tubulin. Compounds 3, 4 and 5 displayed competitive inhibition against colchicine binding, and ...
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(1996)Ca2+ and Gd3+ stimulated the GTPase activity of chicken brain tubulin 13- and 26-fold, respectively. Mg2+, Tb3+, and Na+ had no effect. This GTPase activity showed a saturation behavior with Ca2+ and Gd3+ with a maximal ...
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(Universidad de Chile, 2003)La FtsZ polimeriza para formar el anillo Z alrededor del perímetro transversal en el centro de la célula cuando la bacteria E. coli inicia la formación del septo. En este proceso participan varias proteínas Fts para formar ...
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(Elsevier B.V., 2017)Amyloids are protein aggregates of highly regular structure that are involved in diverse pathologies such as Alzheimer's and Parkinson's disease. Recent evidence has shown that under certain conditions, small peptides can ...
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(COLD SPRING HARBOR LAB PRESS, 2007-08)FtsZ has two domains, the amino GTPase domain with a Rossmann fold, and the carboxyl domain that resembles the chorismate mutase fold. Bioinformatics analyses suggest that the interdomain interaction is stronger than the ...
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(Universidad de ChilePrograma Cybertesis, 2007)FtsZ es una proteína bacteriana esencial en el proceso de división celular. Se localiza en la membrana interna de la célula generando un anillo en la mitad de su eje longitudinal, donde actúa como una proteína de andamiaje ...
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(Frontiers Media SA, 2018)Multiresistant and invasive hypervirulent Klebsiella pneumoniae strains have become one of the most urgent bacterial pathogen threats. Recent analyses revealed a high genomic plasticity of this species, harboring a variety ...
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(2006)The goal of this work was to determine the binding properties and location of 4′,6-diamidino-2-phenylindole (DAPI) complexed with tubulin. Using fluorescence anisotropy, a dissociation constant of 5.2 ± 0.4 μM for the ...
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(BioMed Central Ltd., 2013-02-05)Background: FtsZ is an essential cell division protein, which localizes at the middle of the bacterial cell to mediate cytokinesis. In vitro, FtsZ polymerizes and induces GTPase activity through longitudinal interactions ...
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(1999)We have investigated the solution conformation of the functionally relevant C-terminal extremes of α- and β-tubulin, employing the model recombinant peptides RL52α3 and RL33β6, which correspond to the amino acid sequences ...
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(FEBS, 1999)Acyl-CoAs are present at high concentrations within the cell, yet are strongly buffered by specific binding proteins in order to maintain a low intracellular unbound acyl-CoA concentration, compatible with their metabolic ...
